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Volumn 40, Issue D1, 2012, Pages

NRG-CING: Integrated validation reports of remediated experimental biomolecular NMR data and coordinates in wwPDB

Author keywords

[No Author keywords available]

Indexed keywords

ACCESS TO INFORMATION; ARTICLE; CLIENT SERVER APPLICATION; COMPUTER PROGRAM; HUMAN COMPUTER INTERACTION; INFORMATION PROCESSING; NUCLEAR MAGNETIC RESONANCE RESTRAINTS GRID COMMON INTERFACE FOR NUCLEAR MAGNETIC RESONANCE STRUCTURE GENERATION DATABSE; PRIORITY JOURNAL; PROTEIN DATA BANK; PROTEIN DATABASE; QUALITY CONTROL PROCEDURES; VALIDATION PROCESS; WORLDWIDE PROTEIN DATA BANK;

EID: 84862158668     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr1134     Document Type: Article
Times cited : (32)

References (26)
  • 3
    • 0345059376 scopus 로고    scopus 로고
    • Announcing the worldwide Protein Data Bank
    • DOI 10.1038/nsb1203-980
    • Berman,H., Henrick,K. and Nakamura,H. (2003) Announcing the worldwide Protein Data Bank. Nat. Struct. Biol., 10, 980. (Pubitemid 37500485)
    • (2003) Nature Structural Biology , vol.10 , Issue.12 , pp. 980
    • Berman, H.1    Henrick, K.2    Nakamura, H.3
  • 7
    • 79954611826 scopus 로고    scopus 로고
    • Bayesian estimation of NMR restraint potential and weight: A validation on a representative set of protein structures
    • Bernard,A., Vranken,W.F., Bardiaux,B., Nilges,M. and Malliavin,T.E. (2011) Bayesian estimation of NMR restraint potential and weight: a validation on a representative set of protein structures. Proteins, 79, 1525-1537.
    • (2011) Proteins , vol.79 , pp. 1525-1537
    • Bernard, A.1    Vranken, W.F.2    Bardiaux, B.3    Nilges, M.4    Malliavin, T.E.5
  • 9
    • 58849160465 scopus 로고    scopus 로고
    • Re-refinement from deposited X-ray data can deliver improved models for most PDB entries
    • Joosten,R., Womack,T., Vriend,G. and Bricogne,G. (2009) Re-refinement from deposited X-ray data can deliver improved models for most PDB entries. Acta Cryst. D, 65, 176-185.
    • (2009) Acta Cryst. D , vol.65 , pp. 176-185
    • Joosten, R.1    Womack, T.2    Vriend, G.3    Bricogne, G.4
  • 10
    • 78649817914 scopus 로고    scopus 로고
    • On the complexity of Engh and Huber refinement restraints: The angle t as example
    • Touw,W.G. and Vriend,G. (2010) On the complexity of Engh and Huber refinement restraints: the angle t as example. Acta Crystallogr. D Biol. Crystallogr., 66, 1341-1350.
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 1341-1350
    • Touw, W.G.1    Vriend, G.2
  • 14
    • 23144441604 scopus 로고    scopus 로고
    • BioMagResBank databases DOCR and FRED containing converted and filtered sets of experimental NMR restraints and coordinates from over 500 protein PDB structures
    • DOI 10.1007/s10858-005-2195-0
    • Doreleijers,J.F., Nederveen,A.J., Vranken,W. and Lin,J. (2005) BioMagResBank databases DOCR and FRED containing converted and Eltered sets of experimental NMR restraints and coordinates from over 500 protein PDB structures. J. Biomol. NMR, 32, 1-12. (Pubitemid 41086462)
    • (2005) Journal of Biomolecular NMR , vol.32 , Issue.1 , pp. 1-12
    • Doreleijers, J.F.1    Nederveen, A.J.2    Vranken, W.3    Lin, J.4    Bonvin, A.M.J.J.5    Kaptein, R.6    Markley, J.L.7    Ulrich, E.L.8
  • 15
    • 35848952931 scopus 로고    scopus 로고
    • A global analysis of NMR distance constraints from the PDB
    • Vranken,W. (2007) A global analysis of NMR distance constraints from the PDB. J. Biomol. NMR, 39, 303-314.
    • (2007) J. Biomol. NMR , vol.39 , pp. 303-314
    • Vranken, W.1
  • 16
    • 77955794370 scopus 로고    scopus 로고
    • Validation of archived chemical shifts through atomic coordinates
    • Rieping,W. and Vranken,W.F. (2010) Validation of archived chemical shifts through atomic coordinates. Proteins, 78, 2482-2489.
    • (2010) Proteins , vol.78 , pp. 2482-2489
    • Rieping, W.1    Vranken, W.F.2
  • 17
    • 0037354231 scopus 로고    scopus 로고
    • RefDB: A database of uniformly referenced protein chemical shifts
    • DOI 10.1023/A:1022836027055
    • Zhang,H., Neal,S. and Wishart,D. (2003) RefDB: a database of uniformly referenced protein chemical shifts. J. Biomol. NMR, 25, 173-195. (Pubitemid 36410583)
    • (2003) Journal of Biomolecular NMR , vol.25 , Issue.3 , pp. 173-195
    • Zhang, H.1    Neal, S.2    Wishart, D.S.3
  • 18
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen,Y., Delaglio,F., Cornilescu,G. and Bax,A. (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR, 44, 213-223.
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 20
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch,W. and Sander,C. (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 21
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • Koradi,R., Billeter,M. and Wüthrich,K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph, 14, 51-55. (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 22
    • 0038407231 scopus 로고    scopus 로고
    • 15N chemical shifts
    • DOI 10.1023/A:1023812930288
    • Neal,S., Nip,A., Zhang,H. and Wishart,D. (2003) Rapid and accurate calculation of protein 1H, 13C and 15N chemical shifts. J. Biomol. NMR, 26, 215-240. (Pubitemid 36758442)
    • (2003) Journal of Biomolecular NMR , vol.26 , Issue.3 , pp. 215-240
    • Neal, S.1    Nip, A.M.2    Zhang, H.3    Wishart, D.S.4
  • 23
    • 0036814981 scopus 로고    scopus 로고
    • 13C chemical shift statistics
    • DOI 10.1023/A:1020997118364
    • Schubert,M., Labudde,D., Oschkinat,H. and Schmieder,P. (2002) A software tool for the prediction of Xaa-Pro peptide bond conformations in proteins based on 13C chemical shift statistics. J. Biomol. NMR, 24, 149-154. (Pubitemid 35414678)
    • (2002) Journal of Biomolecular NMR , vol.24 , Issue.2 , pp. 149-154
    • Schubert, M.1    Labudde, D.2    Oschkinat, H.3    Schmieder, P.4
  • 25
    • 70349558318 scopus 로고    scopus 로고
    • Leucine side-chain conformation and dynamics in proteins from 13C NMR chemical shifts
    • Mulder,F. (2009) Leucine side-chain conformation and dynamics in proteins from 13C NMR chemical shifts. Chem. Bio. Chem., 10, 1477-1479.
    • (2009) Chem. Bio. Chem. , vol.10 , pp. 1477-1479
    • Mulder, F.1
  • 26
    • 79956116665 scopus 로고    scopus 로고
    • PDBj Mine: design and implementation of relational database interface for Protein Data Bank Japan
    • doi:10.1093/ database/baq021
    • Kinjo,A.R., Yamashita,R. and Nakamura,H. (2010) PDBj Mine: design and implementation of relational database interface for Protein Data Bank Japan. Database, 2010, doi:10.1093/ database/baq021.
    • (2010) Database, 2010
    • Kinjo, A.R.1    Yamashita, R.2    Nakamura, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.